Native Cow Bovine Serum Albumin Protein

Collections: Antibody / cell therapy targets, Car-t cell therapy targets, Recombinant proteins

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Product Overview

Host Species	Cow
Accession	P02769
Synonym	alb ALBU_HUMAN Albumin Albumin (32 AA) Albumin (AA 34) BSA Cell growth inhibiting protein 42 Growth inhibiting protein 20 PRO0883 PRO0903 PRO1341 Serum albumin
Description	Native Cow Bovine Serum Albumin Protein is native.. It is a Full length protein
Source	Native
AA Sequence	DTHKSEIAHRFKDLGEEHFKGLVLIAFSQYLQQCPFDEHVKLVNELTEFA KTCVADESHAGCEKSLHTLFGDELCKVASLRETYGDMADCCEKQEPERNE CFLSHKDDSPDLPKLKPDPNTLCDEFKADEKKFWGKYLYEIARRHPYFYA PELLYYANKYNGVFQECCQAEDKGACLLPKIETMREKVLASSARQRLRCA SIQKFGERALKAWSVARLSQKFPKAEFVEVTKLVTDLTKVHKECCHGDLL ECADDRADLAKYICDNQDTISSKLKECCDKPLLEKSHCIAEVEKDAIPEN LPPLTADFAEDKDVCKNYQEAKDAFLGSFLYEYSRRHPEYAVSVLLRLAK EYEATLEECCAKDDPHACYSTVFDKLKHLVDEPQNLIKQNCDQFEKLGEY GFQNALIVRYTRKVPQVSTPTLVEVSRSLGKVGTRCCTKPESERMPCTED YLSLILNRLCVLHEKTPVSEKVTKCCTESLVNRRPCFSALTPDETYVPKA FDEKLFTFHADICTLPDTEKQIKKQTALVELLKHKPKATEEQLKTVMENF VAFVDKCCAADDKEACFAVEGPKLVVSTQTALA
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	This product contains:-Moisture: 1.4%Ash: 1.4%Heavy Metals:<0.44ppmBovine IgG:Not detectedProtein: 100% (Biuret)Albumin: 100% (electrophoresis)
Formulation	Lyophilised
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function	Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc. Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (Probable). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner. The shared binding site between zinc and calcium at residue Asp-272 suggests a crosstalk between zinc and calcium transport in the blood (Probable). The rank order of affinity is zinc > calcium > magnesium (Probable). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli. Does not prevent iron uptake by the bacterial siderophore aerobactin.
Subcellular Location	Secreted.
Protein Families	ALB/AFP/VDB family
Database References	KEGG: bta:280717 STRING: 9913.ENSBTAP00000022763 UniGene: Bt.106669
Tissue Specificity	Plasma.

Gene Functions References

The interaction of DRV with bovine serum albumin (BSA), a major carrier protein, has been studied under simulated physiological conditions (pH7.4) by multi-spectroscopic techniques in combination with molecular modeling. PMID: 28753530
hese obtained results provide an in-depth understanding of the interaction of the acid azo dye AO10 with serum albumins. PMID: 29126006
that thiamine hydrochloride (TA) is located in site I of bovine serum albumin (BSA). PMID: 27550086
The molecular dynamics results show how the negatively charged BSA at pH7 adsorbs to the negatively charged silica surface, and reveal a unique orientation with preserved secondary and tertiary structure. The experiments then show that the protein forms complete monolayers at approximately pH6, just above the protein's isoelectric point (pH5.1). PMID: 28350173
Molecular dynamics (MD) simulation results demonstrate that the "hard protein" lysozyme retains much of its secondary structure during adsorption, whereas BSA loses it almost completely. BSA has a considerably larger adsorption energy compared to that of lysozyme, which does not scale with chain length. Desorption simulations are carried out using classical steered MD. PMID: 27421144
identified a total of 125 carbonylated residues in bovine serum albumin after extensive in vitro metal ion-catalysed oxidation PMID: 28062376
Degradation of BSA by serine proteases was monitored with Fourier transform infrared (FT-IR) and ultraviolet circular dichroism (UV-CD). alpha-Helical structure of BSA was converted into unordered structure upon digestion. PMID: 26926394
Data show that the maximum adsorption occurred at the isoelectric point (pH 4.7) of bovine serum albumin (BSA). PMID: 26673525
The ITC results indicated that the interaction between the protein (BSA and BHb) and QDs-612 was spontaneous and the predominant force was hydrophobic interaction PMID: 25143002
Data (including data from biophysical studies using Langmuir lipid monolayer technique) suggest that human/bovine ALB exhibits minimal electrostatic repulsion and inserts effectively into phospholipid monolayers. [REVIEW] PMID: 24267981
data indicate that conjugation of carboxyl groups with monosaccharide generates functional BSA with membrane-perturbing activities on the lipid-water interface. PMID: 25449061
Data suggest that native BSA samples can be dehydrated to approximately 450 waters per protein molecule via microglassification and then reverted to native-like conformation upon rehydration with only minor irreversible aggregation. PMID: 24415208
molecular modeling approaches were employed to determine the interaction between lysionotin and bovine serum albumin (BSA) at physiological pH PMID: 24398555
Bovine Serum Albumine aqueous solutions in the presence of NaCl are investigated for different protein concentrations and low to intermediate ionic strengths. Protein interactions are modeled via a charge-screened colloidal model. PMID: 23534667
A crystallographic structural study allows identification of serum albumin fragments responsible for immunogenicity and the postulation of a mechanism for antigen-antibody recognition in cattle. PMID: 22993082
Glass transition and dynamics in BSA-water mixtures over wide ranges of composition studied by thermal and dielectric techniques. PMID: 21798376
The dynamics of bovine serum albumin (BSA) and human fibrinogen (Fg) at low concentrations were observed at the solid-aqueous interface as a function of temperature. PMID: 22713578
serum albumin possesses chaperone-like properties and that this activity is maintained under a number of physiologically relevant conditions. PMID: 22549788
Interaction between 2',4-dihydroxychalcone and the N, f, e conformers of albumin was exothermic and spontaneous. PMID: 22450828
The results showed that the riboflavin could efficiently bind to BSA in aqueous solution. PMID: 22154267
The unfolding and refolding of BSA appear to proceed through intermediates and both the processes are sequential in nature. PMID: 21993230
The results indicated that the binding abilities of vitamin B12 to BSA in the acidic and basic pH regions (pH 2.5, 3.5, 5.0, and 9.0) were lower than that at simulating physiological condition (pH 7.4). PMID: 21955947
new insights on bovine serum albumin self-assembly process PMID: 21303653
Data indicate that CD spectroscopy of the HSA and BSA released in solution after desorption from the matrices shows that, while both proteins partially regain their helical structure, they show a distinct behaviour in their tertiary structure. PMID: 20692819
Data show that the fluorescence quenching process may occur through energy transfer from singlet excited state of tryptophan in BSA to the corresponding level of ASP. PMID: 20667434
L-Arginine does not prevent amyloid-like fibril formation by BSA. PMID: 20204431
Our data suggest that the efficacy of this detoxication system is based on the high concentration of albumin in plasma (and in the rest of the body), and not on the catalytic efficacy itself, which is low for albumin. PMID: 20211614
The shortest binding distance and energy transfer efficiencies between donor BSA and acceptor methyl pheophorbide-a were obtained by Forster's nonradiative energy transfer mechanism. PMID: 16128079
Data show that the apparent complexation constant of Pb2 x BSA is lgK = 11.61, and the nitrogen in BSA could coordinate with lead in Pb2-BSA. PMID: 15852867
Data show that the binding constants of serum albumin and ZnPc(COOH)16 were 2.25-2.94 x 10(6) L x mol(-1). PMID: 17058928
Data show that the binding power between BLFX and BSA is electrostatic effect. PMID: 17058955
Data show that the combination reaction of AYR with BSA was a static quenching process. PMID: 17058958
Data show that in long interaction period or at high concentration of SDS, SDS unfolded BSA by decreasing the alpha-helix structure and increasing the random coil. PMID: 17112025
Data show that the binding constants (KA) between quercetin and BSA were 2.8 x 10(8) (26 degrees C) and 3.1 x 10(8) (36 degrees C), and the binding sites (n) were 1.7+/-0.02. PMID: 17112044
Data show that the binding constant of this compound with bovine serum albumin (BSA) in aqueous solution was is Ka = 1.995 x 10(5) dm3 x mol(-1) and the binding site number is n = 1.12. PMID: 16201357
results indicated that the binding reaction between BSA and purpure-18-imide was a single static quenching process. PMID: 16097695
Data indicate that the hydrophobic force was the main binding force of TIF with bovine serum albumin in aqueous solution. PMID: 16329500
Data show that the interaction of the umbelliferone-BSA was driven mainly by electrostatic force which was enhanced by Cu2+ and Zn2+. PMID: 16329506
glycation and oxidation effects on the structure of serum albumin; the partial unfolding of the tertiary structure which accompanies the aggregation process is similar both in native and glycated BSA PMID: 20006741
Structural analysis showed that lipids bind BSA via both hydrophilic and hydrophobic contacts. PMID: 19961210
association constant and thermodynamic parameters and binding characterisitics for interaction of nigerloxin with bovine serum albumin. PMID: 15134145
Temperature-dependent secondary structure and conformational changes to serum albumin occur twice, around 57 and 75 degrees C., and reveal that the alpha-helix and turn structures of serum albumin are cooperatively denatured by heating. PMID: 15350138
Albumin up-regulates ligand-binding TGF-beta receptors on cultured proximal tubular cells. Albumin-induced activation of local Ang II production appears to be responsible for this effect. PMID: 15496155
The results from the models show that there are at least two different binding sites located in the BSA protein with different water accessibility PMID: 16382334
Human preadipocytes and freshly isolated adipocytes incubated with bovine serum albumin (BSA) in vitro secrete significantly higher amounts of cytokines IL-6, -8, and -10, and TNF-alpha compared with cells incubated without BSA. PMID: 16452161
Serum albumin and serum retinol-binding protein(sRBP) are not components of bovine interphotoreceptor matrix(IPM). Serum albumin and sRBP can not participate in binding and transport of visual cycle retinoids in IPM of bovine retina. PMID: 17200663
Bovine serum albumin is common allergen responsible for cow's milk allergy. Cross reactivity with serum albumins in meat/epithelial cells of other mammals results. PMID: 17680908
BSA is able to form well-ordered beta-sheet rich aggregates which nevertheless do not possess the same structural rigidity as classical fibrils. PMID: 17689306
interaction of bovine serum albumin with isoxazolcurcumin and diacetylcurcumin yielded binding constants, minor BSA conformation changes, and binding site PMID: 18037556
The present study shows that GM1 has a strong effect on the conformation of BSA depending on the conformational states of the protein that would relate to a physiological function of GM1 such as acting as the receptor of proteins in the cell membrane. PMID: 18205315

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.